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. 1972 Mar;1(3):242–246. doi: 10.1128/aac.1.3.242

Origin of Glycine from Acid Hydrolysis of the β-Lactam Antibiotic A16886B

D R Brannon 1, J A Mabe 1, R Ellis 1, J G Whitney 1, R Nagarajan 1
PMCID: PMC444199  PMID: 5045470

Abstract

Structural analysis of two new β-lactam antibiotics, A16884A and A16886B, indicated that they, like cephalosporin C, were composed of modified valine and cysteine residues, and α-aminoadipic acid. However, acid hydrolysis of A16886B and A16884A produced three times as much glycine as did hydrolysis of cephalosporin C under the same conditions. Samples of A16886B-14C-6 and A16886B-14C-8 were prepared by the addition of cysteine-14C-3 and cystine-14C-1 to fermentations of Streptomyces clavuligerus. The specific activity of glycine obtained from hydrolysis of A16886B-14C-6 was considerably higher than that from hydrolysis of A16886B-14C-8. An explanation for the difference in amounts of glycine obtained from hydrolysis of these antibiotics is discussed.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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